Potassium voltage-gated channel subfamily E member 3

Details

Name
Potassium voltage-gated channel subfamily E member 3
Synonyms
  • Minimum potassium ion channel-related peptide 2
  • MinK-related peptide 2
  • Potassium channel subunit beta MiRP2
Gene Name
KCNE3
Organism
Humans
Amino acid sequence
>lcl|BSEQ0052259|Potassium voltage-gated channel subfamily E member 3
METTNGTETWYESLHAVLKALNATLHSNLLCRPGPGLGPDNQTEERRASLPGRDDNSYMY
ILFVMFLFAVTVGSLILGYTRSRKVDKRSDPYHVYIKNRVSMI
Number of residues
103
Molecular Weight
11710.3
Theoretical pI
Not Available
GO Classification
Functions
ion channel binding / potassium channel regulator activity / voltage-gated potassium channel activity
Processes
membrane repolarization during action potential / membrane repolarization during ventricular cardiac muscle cell action potential / negative regulation of delayed rectifier potassium channel activity / negative regulation of membrane repolarization during ventricular cardiac muscle cell action potential / negative regulation of potassium ion export across plasma membrane / negative regulation of voltage-gated potassium channel activity / positive regulation of voltage-gated calcium channel activity / potassium ion export across plasma membrane / regulation of heart rate by cardiac conduction / regulation of ventricular cardiac muscle cell membrane repolarization / ventricular cardiac muscle cell action potential
Components
cytoplasm / dendrite / membrane raft / neuronal cell body membrane / perikaryon / vesicle / voltage-gated potassium channel complex
General Function
Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 (PubMed:12954870). Associated with KCNC4/Kv3.4 is proposed to form the subthreshold voltage-gated potassium channel in skeletal muscle and to establish the resting membrane potential (RMP) in muscle cells. Associated with KCNQ1/KCLQT1 may form the intestinal cAMP-stimulated potassium channel involved in chloride secretion that produces a current with nearly instantaneous activation with a linear current-voltage relationship.
Specific Function
Ion channel binding
Pfam Domain Function
Transmembrane Regions
58-78
Cellular Location
Cell membrane
Gene sequence
>lcl|BSEQ0052260|Potassium voltage-gated channel subfamily E member 3 (KCNE3)
ATGGAGACTACCAATGGAACGGAGACCTGGTATGAGAGCCTGCATGCCGTGCTGAAGGCT
CTAAATGCCACTCTTCACAGCAATTTGCTCTGCCGGCCAGGGCCAGGGCTGGGGCCAGAC
AACCAGACTGAAGAGAGGCGGGCCAGCCTACCTGGCCGTGATGACAACTCCTACATGTAC
ATTCTCTTTGTCATGTTTCTATTTGCTGTAACTGTGGGCAGCCTCATCCTGGGATACACC
CGCTCCCGCAAAGTGGACAAGCGTAGTGACCCCTATCATGTGTATATCAAGAACCGTGTG
TCTATGATCTAA
Chromosome Location
11
Locus
11q13.4
External Identifiers
ResourceLink
UniProtKB IDQ9Y6H6
UniProtKB Entry NameKCNE3_HUMAN
HGNC IDHGNC:6243
General References
  1. Melman YF, Domenech A, de la Luna S, McDonald TV: Structural determinants of KvLQT1 control by the KCNE family of proteins. J Biol Chem. 2001 Mar 2;276(9):6439-44. doi: 10.1074/jbc.M010713200. Epub 2000 Dec 4. [Article]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  3. Schroeder BC, Waldegger S, Fehr S, Bleich M, Warth R, Greger R, Jentsch TJ: A constitutively open potassium channel formed by KCNQ1 and KCNE3. Nature. 2000 Jan 13;403(6766):196-9. [Article]
  4. Abbott GW, Butler MH, Bendahhou S, Dalakas MC, Ptacek LJ, Goldstein SA: MiRP2 forms potassium channels in skeletal muscle with Kv3.4 and is associated with periodic paralysis. Cell. 2001 Jan 26;104(2):217-31. doi: 10.1016/s0092-8674(01)00207-0. [Article]
  5. Abbott GW, Goldstein SA: Disease-associated mutations in KCNE potassium channel subunits (MiRPs) reveal promiscuous disruption of multiple currents and conservation of mechanism. FASEB J. 2002 Mar;16(3):390-400. [Article]
  6. McCrossan ZA, Lewis A, Panaghie G, Jordan PN, Christini DJ, Lerner DJ, Abbott GW: MinK-related peptide 2 modulates Kv2.1 and Kv3.1 potassium channels in mammalian brain. J Neurosci. 2003 Sep 3;23(22):8077-91. [Article]
  7. Roura-Ferrer M, Sole L, Oliveras A, Dahan R, Bielanska J, Villarroel A, Comes N, Felipe A: Impact of KCNE subunits on KCNQ1 (Kv7.1) channel membrane surface targeting. J Cell Physiol. 2010 Nov;225(3):692-700. doi: 10.1002/jcp.22265. [Article]
  8. Dias Da Silva MR, Cerutti JM, Arnaldi LA, Maciel RM: A mutation in the KCNE3 potassium channel gene is associated with susceptibility to thyrotoxic hypokalemic periodic paralysis. J Clin Endocrinol Metab. 2002 Nov;87(11):4881-4. doi: 10.1210/jc.2002-020698. [Article]
  9. Sternberg D, Tabti N, Fournier E, Hainque B, Fontaine B: Lack of association of the potassium channel-associated peptide MiRP2-R83H variant with periodic paralysis. Neurology. 2003 Sep 23;61(6):857-9. doi: 10.1212/01.wnl.0000082392.66713.e3. [Article]
  10. Jurkat-Rott K, Lehmann-Horn F: Periodic paralysis mutation MiRP2-R83H in controls: Interpretations and general recommendation. Neurology. 2004 Mar 23;62(6):1012-5. doi: 10.1212/01.wnl.0000119392.29624.88. [Article]
  11. Delpon E, Cordeiro JM, Nunez L, Thomsen PE, Guerchicoff A, Pollevick GD, Wu Y, Kanters JK, Larsen CT, Hofman-Bang J, Burashnikov E, Christiansen M, Antzelevitch C: Functional effects of KCNE3 mutation and its role in the development of Brugada syndrome. Circ Arrhythm Electrophysiol. 2008 Aug;1(3):209-18. doi: 10.1161/CIRCEP.107.748103. [Article]
  12. Ohno S, Toyoda F, Zankov DP, Yoshida H, Makiyama T, Tsuji K, Honda T, Obayashi K, Ueyama H, Shimizu W, Miyamoto Y, Kamakura S, Matsuura H, Kita T, Horie M: Novel KCNE3 mutation reduces repolarizing potassium current and associated with long QT syndrome. Hum Mutat. 2009 Apr;30(4):557-63. doi: 10.1002/humu.20834. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00228Enfluraneapproved, investigational, vet_approvedunknowninhibitoractivatorDetails
DB01069Promethazineapproved, investigationalunknowninducerDetails
DB01110Miconazoleapproved, investigational, vet_approvedunknowninhibitorDetails